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Literature summary for 4.2.1.119 extracted from
- Characterization and functional analyses of R-specific enoyl coenzyme A hydratases in polyhydroxyalkanoate-producing Ralstonia eutropha (2012), Appl. Environ. Microbiol., 78, 493-502.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression of the three His6-tagged PhaJ4 homologues individually in Escherichia coli strain BL21(DE3) | Cupriavidus necator |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | engineered Ralstonia eutropha strains as host strains for PhaJ4aRe to PhaJ4cRe are capable of synthesizing poly((R)-3-hydroxybutyrate-co-(R)-3-hydroxyhexanoate) from soybean oil due to modifications enabling the biosynthesis of P(3HB-co-3HHx) composed of a larger 3HHx fraction without a negative impact on cell growth and PHA production on soybean oil, especially when phaJ4aRe or phaJ4bRe is tandemly introduced with phaJAc from Aeromonas caviae. Introduction of phaJ4aRe or phaJ4bRe into the Ralstonia eutropha strains using a broad-host-range vector enhances the 3HHx composition of the copolyesters, but the introduction of phaJ4cRe does not | Cupriavidus necator |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic parameters of recombinant PhaJ4aRe to PhaJ4cRe or hydration toward trans-2-enoyl-CoAs of C4 to C8 and comparison to those of PhaJ4Pa and PhaJAc, overview | Cupriavidus necator | |
| additional information | - |
additional information | kinetic parameters of recombinant PhaJ4aRe to PhaJ4cRe or hydration toward trans-2-enoyl-CoAs of C4 to C8 and comparison to those of PhaJ4Pa and PhaJAc, overview | Pseudomonas aeruginosa |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 16500 | - |
x * 17500, recombinant isozyme His-tagged PhaJ4aRe, SDS-PAGE, x * 17000, recombinant His-tagged PhaJ4bRe, SDS-PAGE, x * 16500, recombinant His-tagged PhaJ4cRe, SDS-PAGE | Cupriavidus necator |
| 17000 | - |
x * 17500, recombinant isozyme His-tagged PhaJ4aRe, SDS-PAGE, x * 17000, recombinant His-tagged PhaJ4bRe, SDS-PAGE, x * 16500, recombinant His-tagged PhaJ4cRe, SDS-PAGE | Cupriavidus necator |
| 17500 | - |
x * 17500, recombinant isozyme His-tagged PhaJ4aRe, SDS-PAGE, x * 17000, recombinant His-tagged PhaJ4bRe, SDS-PAGE, x * 16500, recombinant His-tagged PhaJ4cRe, SDS-PAGE | Cupriavidus necator |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (3R)-3-hydroxyacyl-CoA | Cupriavidus necator | - |
(2E)-2-enoyl-CoA + H2O | - |
? |  |
| (3R)-3-hydroxyacyl-CoA | Pseudomonas aeruginosa | - |
(2E)-2-enoyl-CoA + H2O | - |
? | |
| (3R)-3-hydroxyacyl-CoA | Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | - |
(2E)-2-enoyl-CoA + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cupriavidus necator | - |
presence of 16 orthologues of R-specific enoyl-CoA hydratase, among which three proteins shares high homologies with the enzyme specific to enoyl-CoAs of medium chain length encoded by phaJ4 from Pseudomonas aeruginosa | - |
| Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | - |
presence of 16 orthologues of R-specific enoyl-CoA hydratase, among which three proteins shares high homologies with the enzyme specific to enoyl-CoAs of medium chain length encoded by phaJ4 from Pseudomonas aeruginosa | - |
| Pseudomonas aeruginosa | Q9HX12 | gene phaJ4 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged PhaJ4 homologues from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Cupriavidus necator |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (3R)-3-hydroxyacyl-CoA | - |
Cupriavidus necator | (2E)-2-enoyl-CoA + H2O | - |
? | |
| (3R)-3-hydroxyacyl-CoA | - |
Pseudomonas aeruginosa | (2E)-2-enoyl-CoA + H2O | - |
? | |
| (3R)-3-hydroxyacyl-CoA | recombinant forms of the three proteins, PhaJ4aRe to PhaJ4cRe, show enoyl-CoA hydratase activity with R specificity, and the catalytic efficiencies are elevated as the substrate chain length increases from C4 to C8. PhaJ4aRe and PhaJ4bRe show over 10fold higher catalytic efficiency than PhaJ4cRe | Cupriavidus necator | (2E)-2-enoyl-CoA + H2O | - |
? | |
| (3R)-3-hydroxyacyl-CoA | - |
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | (2E)-2-enoyl-CoA + H2O | - |
? | |
| (3R)-3-hydroxyacyl-CoA | recombinant forms of the three proteins, PhaJ4aRe to PhaJ4cRe, show enoyl-CoA hydratase activity with R specificity, and the catalytic efficiencies are elevated as the substrate chain length increases from C4 to C8. PhaJ4aRe and PhaJ4bRe show over 10fold higher catalytic efficiency than PhaJ4cRe | Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | (2E)-2-enoyl-CoA + H2O | - |
? | |
| additional information | engineered Ralstonia eutropha strains as host strains for PhaJ4aRe to PhaJ4cRe are capable of synthesizing poly((R)-3-hydroxybutyrate-co-(R)-3-hydroxyhexanoate) from soybean oil, but only PhaJ4aRe is one of the major enzymes supplying the (R)-3-hydroxyhexanoate-CoA monomer through beta-oxidation, pathway overview | Cupriavidus necator | ? | - |
? | |
| additional information | the enzyme is specific for enoyl-CoAs of medium chain length | Pseudomonas aeruginosa | ? | - |
? | |
| additional information | engineered Ralstonia eutropha strains as host strains for PhaJ4aRe to PhaJ4cRe are capable of synthesizing poly((R)-3-hydroxybutyrate-co-(R)-3-hydroxyhexanoate) from soybean oil, but only PhaJ4aRe is one of the major enzymes supplying the (R)-3-hydroxyhexanoate-CoA monomer through beta-oxidation, pathway overview | Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 17500, recombinant isozyme His-tagged PhaJ4aRe, SDS-PAGE, x * 17000, recombinant His-tagged PhaJ4bRe, SDS-PAGE, x * 16500, recombinant His-tagged PhaJ4cRe, SDS-PAGE | Cupriavidus necator |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PhaJ4 | - |
Pseudomonas aeruginosa |
| PhaJ4aRe | - |
Cupriavidus necator |
| PhaJ4bRe | - |
Cupriavidus necator |
| PhaJ4cRe | - |
Cupriavidus necator |
| R-specific enoyl coenzyme A hydratase | - |
Cupriavidus necator |
| R-specific enoyl coenzyme A hydratase | - |
Pseudomonas aeruginosa |
| R-specific enoyl-CoA hydratase | - |
Cupriavidus necator |
| R-specific enoyl-CoA hydratase | - |
Pseudomonas aeruginosa |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Cupriavidus necator |
| 30 | - |
assay at | Pseudomonas aeruginosa |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Cupriavidus necator |
| 7.5 | - |
assay at | Pseudomonas aeruginosa |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | phylogenetic tree of MaoC-like domains in PhaJ homologues encoded in Ralstonia eutropha H16 genome and domains in the known PhaJ proteins from Aeromonas caviae and Pseudomonas aeruginosa | Cupriavidus necator |
| evolution | phylogenetic tree of MaoC-like domains in PhaJ homologues encoded in Ralstonia eutropha H16 genome and domains in the known PhaJ proteins from Aeromonas caviae and Pseudomonas aeruginosa | Pseudomonas aeruginosa |
| malfunction | deletion of phaJ4aRe from the chromosome results in significant decrease of (R)-3-hydroxyhexanoate composition in the accumulated copolyester, whereas no change is observed with deletion of phaJ4bRe or phaJ4cRe | Cupriavidus necator |
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